Results 31 to 40 of about 182,890 (341)
Considering the biological and ecological importance of Cu–thiol interactions and the discrepancies in previous research, this study focuses on Cu interactions with biologically and ecologically relevant thiols: glutathione (GSH), L-cysteine (L-cys), 3 ...
Dora Crmarić, Elvira Bura-Nakić
doaj +1 more source
ROLE OF THIOLS IN OXIDATIVE STRESS
A well-regulated redox state is essential for normal physiological function and cellular metabolism. In most eukaryotic cells, protein cysteine thiols are most sensitive to fluctuations in the cellular redox state.
S. Baba, A. Bhatnagar
semanticscholar +1 more source
An efficient synthesis of α-(1,3,5-triazinylthio)-ketones from 1,3-dicarbonyl compounds with 1,3,5-triazine-2-thiols has been developed. The reaction proceeds through the C–C bond cleavage and C–S bond reconstruction of 1,3-dicarbonyl compounds, and β ...
Cheng Zhang (70708) +11 more
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The cytochrome bd oxidase catalyzes the reduction of oxygen to water in bacteria and it is thus an interesting target for electrocatalytic studies and biosensor applications. The bd oxidase is completely embedded in the phospholipid membrane.
Anton Nikolaev +6 more
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Although Michael acceptors display a potent and broad spectrum of bioactivity, they have largely been ignored in drug discovery because of their presumed indiscriminate reactivity.
P. Jackson +3 more
semanticscholar +1 more source
An XPS investigation into the chemical composition of metal surfaces modified by the individual cure components of anaerobic adhesives and functionalised thiols [PDF]
This thesis investigates the application of surface sensitive techniques to analyse the chemical composition of metal surfaces modified by a variety of surface treatments.
Stewart, Clodagh Michele
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Introduction. Pemphigus vulgaris (PV) is a life-threatening disease of the skin and mucous membranes that is associated with IgG antibodies that target several types of keratinocyte antigens and cause epidermal lysis (acantholysis) via intracellular ...
V. A. Litvinov, H. I. Makurina
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The Basics of Thiols and Cysteines in Redox Biology and Chemistry
Cysteine is one of the least abundant amino acids, yet it is frequently found as a highly conserved residue within functional (regulatory, catalytic or binding) sites in proteins. It is the unique chemistry of the thiol or thiolate group of cysteine that
L. Poole
semanticscholar +1 more source
Total half-cystine residues in proteins of pig liver chromatin have been measured. About half of them are present in the reduced state. Thiol groups of non-historic chromatin proteins, which amount to about 40 nmol/mg of protein, are preferentially located in chromatin fragments which are more easily solubilised either by DNAse I or by DNAse II.
FERRARO, Anna +5 more
openaire +3 more sources
The first example of palladium-catalyzed cycloisomerization of (Z)-2-en-4-yne-1-thiols 1 to give substituted thiophenes 2 is reported. Cycloisomerization reactions are carried out under nitrogen at 25−100 °C in N,N-dimethylacetamide as the solvent in the
Alessia Fazio (2714503) +2 more
core +2 more sources

